HEADER HYDROLASE/IMMUNE SYSTEM 02-SEP-10 3OPZ
TITLE CRYSTAL STRUCTURE OF TRANS-SIALIDASE IN COMPLEX WITH THE FAB FRAGMENT
TITLE 2 OF A NEUTRALIZING MONOCLONAL IGG ANTIBODY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANS-SIALIDASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.2.1.18;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HEAVY CHAIN OF THE FAB FRAGMENT OF IMMUNOGLOBULIN G;
COMPND 9 CHAIN: H, I, J;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: LIGHT CHAIN OF THE FAB FRAGMENT OF IMMUNOGLOBULIN G;
COMPND 12 CHAIN: L, M, N
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 5693;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TOP10F;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTRCHISA;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 STRAIN: C3H/HEJ;
SOURCE 14 OTHER_DETAILS: MONOCLONAL ANTIBODY WAS OBTAINED FROM HYBRIDOMAS
SOURCE 15 (AFTER FUSION OF MICE SPLENOCYTES WITH SP2/0 CELLS), AND THE FAB
SOURCE 16 FRAGMENT OBTAINED BY STANDARD PAPAIN DIGESTION;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 19 ORGANISM_COMMON: MOUSE;
SOURCE 20 ORGANISM_TAXID: 10090;
SOURCE 21 STRAIN: C3H/HEJ;
SOURCE 22 OTHER_DETAILS: MONOCLONAL ANTIBODY WAS OBTAINED FROM HYBRIDOMAS
SOURCE 23 (AFTER FUSION OF MICE SPLENOCYTES WITH SP2/0 CELLS), AND THE FAB
SOURCE 24 FRAGMENT OBTAINED BY STANDARD PAPAIN DIGESTION
KEYWDS SIX-BLADED BETA-PROPELLER NEURAMINIDASE IMMUNOGLOBULIN DOMAIN, VIRAL
KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX, HYDROLASE-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.LARRIEUX,R.MUIA,O.CAMPETELLA,A.BUSCHIAZZO
REVDAT 3 06-OCT-21 3OPZ 1 REMARK DBREF SEQADV
REVDAT 2 07-MAR-12 3OPZ 1 JRNL
REVDAT 1 09-NOV-11 3OPZ 0
JRNL AUTH A.BUSCHIAZZO,R.MUIA,N.LARRIEUX,T.PITCOVSKY,J.MUCCI,
JRNL AUTH 2 O.CAMPETELLA
JRNL TITL TRYPANOSOMA CRUZI TRANS-SIALIDASE IN COMPLEX WITH A
JRNL TITL 2 NEUTRALIZING ANTIBODY: STRUCTURE/FUNCTION STUDIES TOWARDS
JRNL TITL 3 THE RATIONAL DESIGN OF INHIBITORS.
JRNL REF PLOS PATHOG. V. 8 02474 2012
JRNL REFN ISSN 1553-7366
JRNL PMID 22241998
JRNL DOI 10.1371/JOURNAL.PPAT.1002474
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 68587
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1014
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4974
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24414
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 42
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : -0.17000
REMARK 3 B12 (A**2) : 0.06000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.422
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.316
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.979
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25030 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34035 ; 1.527 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3158 ; 6.682 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1022 ;37.130 ;23.806
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4033 ;18.703 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 123 ;18.633 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3790 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18855 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 633 1
REMARK 3 1 B 1 B 633 1
REMARK 3 1 C 1 C 633 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : L M N
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 2 L 212 1
REMARK 3 1 M 2 M 212 1
REMARK 3 1 N 2 N 212 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : H I J
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 2 H 222 1
REMARK 3 1 I 2 I 222 1
REMARK 3 1 J 2 J 222 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 633
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6080 14.3470 0.2560
REMARK 3 T TENSOR
REMARK 3 T11: 0.1813 T22: 0.0865
REMARK 3 T33: 0.0920 T12: 0.0179
REMARK 3 T13: 0.0080 T23: -0.0814
REMARK 3 L TENSOR
REMARK 3 L11: 1.1604 L22: 0.9099
REMARK 3 L33: 1.6799 L12: 0.3800
REMARK 3 L13: -0.6646 L23: -0.5634
REMARK 3 S TENSOR
REMARK 3 S11: 0.1003 S12: -0.1939 S13: 0.1630
REMARK 3 S21: 0.0378 S22: -0.0331 S23: -0.0576
REMARK 3 S31: 0.0079 S32: 0.1691 S33: -0.0671
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 633
REMARK 3 ORIGIN FOR THE GROUP (A): 86.5840 31.3660 -35.1240
REMARK 3 T TENSOR
REMARK 3 T11: 0.2164 T22: 0.1804
REMARK 3 T33: 0.1333 T12: -0.1047
REMARK 3 T13: -0.1481 T23: 0.1090
REMARK 3 L TENSOR
REMARK 3 L11: 1.0307 L22: 1.4894
REMARK 3 L33: 1.5560 L12: 0.1451
REMARK 3 L13: 0.1887 L23: 0.6295
REMARK 3 S TENSOR
REMARK 3 S11: 0.2031 S12: -0.2889 S13: -0.1434
REMARK 3 S21: -0.0199 S22: -0.0373 S23: 0.1359
REMARK 3 S31: 0.1800 S32: -0.1383 S33: -0.1659
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 633
REMARK 3 ORIGIN FOR THE GROUP (A): 71.8870 -41.2160 3.4970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2326 T22: 0.1809
REMARK 3 T33: 0.3356 T12: 0.0079
REMARK 3 T13: -0.0947 T23: 0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 1.7513 L22: 0.6920
REMARK 3 L33: 1.5382 L12: -0.1354
REMARK 3 L13: -0.9279 L23: 0.1788
REMARK 3 S TENSOR
REMARK 3 S11: -0.0390 S12: 0.2614 S13: 0.1718
REMARK 3 S21: -0.0822 S22: -0.0308 S23: 0.0627
REMARK 3 S31: -0.0957 S32: -0.2482 S33: 0.0698
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 106
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4840 0.2960 -33.3700
REMARK 3 T TENSOR
REMARK 3 T11: 0.1000 T22: 0.2218
REMARK 3 T33: 0.2248 T12: 0.0812
REMARK 3 T13: 0.0134 T23: -0.0820
REMARK 3 L TENSOR
REMARK 3 L11: 1.2980 L22: 3.0271
REMARK 3 L33: 4.7619 L12: 1.5384
REMARK 3 L13: 0.7932 L23: 2.7113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0292 S12: 0.0584 S13: -0.0934
REMARK 3 S21: 0.0669 S22: -0.1412 S23: 0.2664
REMARK 3 S31: 0.1526 S32: -0.2157 S33: 0.1120
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 107 L 212
REMARK 3 ORIGIN FOR THE GROUP (A): 54.1360 -28.3800 -47.3360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1629 T22: 0.3385
REMARK 3 T33: 0.1886 T12: 0.0763
REMARK 3 T13: 0.0200 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 6.5360 L22: 3.2798
REMARK 3 L33: 2.0284 L12: -1.8450
REMARK 3 L13: 1.9288 L23: 0.7249
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: -0.3430 S13: -0.6429
REMARK 3 S21: 0.0578 S22: 0.0475 S23: 0.1647
REMARK 3 S31: 0.3746 S32: 0.0421 S33: -0.0511
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 2 H 118
REMARK 3 ORIGIN FOR THE GROUP (A): 54.1520 5.4170 -23.4210
REMARK 3 T TENSOR
REMARK 3 T11: 0.1517 T22: 0.4012
REMARK 3 T33: 0.1907 T12: 0.0306
REMARK 3 T13: 0.0254 T23: -0.1372
REMARK 3 L TENSOR
REMARK 3 L11: 4.3921 L22: 5.5084
REMARK 3 L33: 4.0728 L12: -3.0150
REMARK 3 L13: 0.2828 L23: 1.5350
REMARK 3 S TENSOR
REMARK 3 S11: 0.1355 S12: -0.1228 S13: 0.3676
REMARK 3 S21: 0.1646 S22: 0.0506 S23: -0.3562
REMARK 3 S31: -0.0683 S32: 0.8126 S33: -0.1861
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 119 H 222
REMARK 3 ORIGIN FOR THE GROUP (A): 64.5910 -16.6910 -48.5930
REMARK 3 T TENSOR
REMARK 3 T11: 0.0677 T22: 0.3327
REMARK 3 T33: 0.3347 T12: 0.0496
REMARK 3 T13: 0.0245 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 3.9994 L22: 5.0881
REMARK 3 L33: 9.4820 L12: -0.8467
REMARK 3 L13: 0.7225 L23: 1.8462
REMARK 3 S TENSOR
REMARK 3 S11: -0.1525 S12: 0.2084 S13: 0.2248
REMARK 3 S21: -0.3671 S22: 0.1889 S23: -0.1652
REMARK 3 S31: 0.0207 S32: -0.0391 S33: -0.0364
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 106
REMARK 3 ORIGIN FOR THE GROUP (A): 61.7780 29.0050 -68.8030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1861 T22: 0.1775
REMARK 3 T33: 0.1923 T12: -0.0725
REMARK 3 T13: -0.1272 T23: 0.1070
REMARK 3 L TENSOR
REMARK 3 L11: 2.9883 L22: 4.2698
REMARK 3 L33: 2.7814 L12: -0.7496
REMARK 3 L13: 1.7138 L23: -2.1559
REMARK 3 S TENSOR
REMARK 3 S11: 0.3899 S12: 0.0796 S13: -0.1128
REMARK 3 S21: -0.1145 S22: -0.1280 S23: 0.1364
REMARK 3 S31: 0.1992 S32: -0.2423 S33: -0.2618
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 107 M 212
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0800 37.9110 -83.9530
REMARK 3 T TENSOR
REMARK 3 T11: 0.2587 T22: 0.4510
REMARK 3 T33: 0.2658 T12: -0.0647
REMARK 3 T13: -0.0645 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 6.3630 L22: 3.3658
REMARK 3 L33: 2.1127 L12: 1.0126
REMARK 3 L13: -0.4443 L23: -0.7111
REMARK 3 S TENSOR
REMARK 3 S11: 0.3455 S12: -0.1227 S13: 0.2179
REMARK 3 S21: -0.0265 S22: -0.2316 S23: 0.5665
REMARK 3 S31: 0.0175 S32: -0.6408 S33: -0.1139
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 4 I 118
REMARK 3 ORIGIN FOR THE GROUP (A): 50.4950 13.0770 -59.2390
REMARK 3 T TENSOR
REMARK 3 T11: 0.8007 T22: 0.5188
REMARK 3 T33: 0.5172 T12: -0.5089
REMARK 3 T13: -0.2980 T23: 0.3101
REMARK 3 L TENSOR
REMARK 3 L11: 7.6962 L22: 1.3800
REMARK 3 L33: 3.0338 L12: 0.8831
REMARK 3 L13: 3.0719 L23: -1.0050
REMARK 3 S TENSOR
REMARK 3 S11: 0.6777 S12: -0.6073 S13: -1.0142
REMARK 3 S21: 0.0656 S22: 0.0757 S23: 0.1714
REMARK 3 S31: 0.7679 S32: -0.7279 S33: -0.7533
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 119 I 219
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4670 22.3650 -85.2290
REMARK 3 T TENSOR
REMARK 3 T11: 0.4412 T22: 0.3968
REMARK 3 T33: 0.5207 T12: -0.1784
REMARK 3 T13: -0.1487 T23: -0.0540
REMARK 3 L TENSOR
REMARK 3 L11: 6.5314 L22: 3.1988
REMARK 3 L33: 9.2308 L12: 1.5190
REMARK 3 L13: -1.5735 L23: -2.1195
REMARK 3 S TENSOR
REMARK 3 S11: 0.1611 S12: 0.2600 S13: -0.6911
REMARK 3 S21: -0.5476 S22: -0.0353 S23: -0.0151
REMARK 3 S31: 0.5758 S32: -0.5439 S33: -0.1257
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 106
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4970 -59.7600 36.5930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1205 T22: 0.3403
REMARK 3 T33: 0.4511 T12: -0.1056
REMARK 3 T13: -0.0552 T23: -0.0685
REMARK 3 L TENSOR
REMARK 3 L11: 2.4421 L22: 4.3015
REMARK 3 L33: 2.4072 L12: -2.1315
REMARK 3 L13: 0.1027 L23: -2.0183
REMARK 3 S TENSOR
REMARK 3 S11: -0.1112 S12: -0.1946 S13: -0.1918
REMARK 3 S21: 0.2820 S22: -0.0596 S23: -0.0698
REMARK 3 S31: 0.0880 S32: -0.2684 S33: 0.1708
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 107 N 212
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5210 -92.0660 50.4770
REMARK 3 T TENSOR
REMARK 3 T11: 0.6518 T22: 0.8631
REMARK 3 T33: 1.3002 T12: -0.3419
REMARK 3 T13: -0.1898 T23: 0.2014
REMARK 3 L TENSOR
REMARK 3 L11: 0.9531 L22: 1.8491
REMARK 3 L33: 2.6115 L12: -1.2709
REMARK 3 L13: 0.4757 L23: -0.2078
REMARK 3 S TENSOR
REMARK 3 S11: 0.1953 S12: -0.2587 S13: -0.7034
REMARK 3 S21: -0.0089 S22: 0.3991 S23: 0.6940
REMARK 3 S31: 0.9190 S32: -0.8044 S33: -0.5944
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 2 J 118
REMARK 3 ORIGIN FOR THE GROUP (A): 35.1840 -59.0910 26.6860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1665 T22: 0.5624
REMARK 3 T33: 0.5363 T12: -0.0099
REMARK 3 T13: -0.0271 T23: -0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 3.7166 L22: 4.3000
REMARK 3 L33: 3.9523 L12: 1.5676
REMARK 3 L13: 0.0285 L23: -2.4015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0804 S12: -0.0202 S13: 0.0567
REMARK 3 S21: 0.0356 S22: -0.0383 S23: 0.5052
REMARK 3 S31: -0.1999 S32: -0.7778 S33: -0.0421
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 119 J 219
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2880 -82.2050 51.6740
REMARK 3 T TENSOR
REMARK 3 T11: 0.4690 T22: 1.3815
REMARK 3 T33: 1.2887 T12: -0.2361
REMARK 3 T13: 0.1462 T23: 0.3196
REMARK 3 L TENSOR
REMARK 3 L11: 3.3926 L22: 2.2553
REMARK 3 L33: 9.7014 L12: -0.8639
REMARK 3 L13: 5.0845 L23: -0.9976
REMARK 3 S TENSOR
REMARK 3 S11: 0.0903 S12: -0.9570 S13: -0.7619
REMARK 3 S21: 0.3209 S22: 0.6934 S23: 0.8561
REMARK 3 S31: 0.4843 S32: -0.9796 S33: -0.7837
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS COMPONENT INCLUDED
REMARK 4
REMARK 4 3OPZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 108
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MULTILAYER MIRRORS (VARIMAX HF)
REMARK 200 OPTICS : VARIMAX HF MULTILAYER MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.9
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68611
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 154.273
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.19000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.51600
REMARK 200 R SYM FOR SHELL (I) : 0.51600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINA, 10 % PEG 20000, 4% 1,4
REMARK 280 -DIOXANO, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.90333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 93.80667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETEROTRIMER, WITH THREE
REMARK 300 TRIMERS IN THE ASU (CHAINS A-H-L, B-I-M AND C-J-N). EACH
REMARK 300 HETEROTRIMERS CORRESPONDS TO A STABLE BINARY COMPLEX BETWEEN TRANS-
REMARK 300 SIALIDASE (E.G. CHAIN A) AND A FAB IGG FRAGMENT, ITSELF A
REMARK 300 HETERODIMER (CHAINS H AND L).
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I, M
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, J, N
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -13
REMARK 465 GLY A -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 GLY A -3
REMARK 465 MET A -2
REMARK 465 ALA A -1
REMARK 465 ASP A 400
REMARK 465 PRO A 401
REMARK 465 ALA A 402
REMARK 465 ALA A 403
REMARK 465 SER A 404
REMARK 465 SER A 405
REMARK 465 SER A 406
REMARK 465 GLU A 407
REMARK 465 ARG A 408
REMARK 465 ASP A 634
REMARK 465 MET B -13
REMARK 465 GLY B -12
REMARK 465 GLY B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 GLY B -3
REMARK 465 MET B -2
REMARK 465 ALA B -1
REMARK 465 ASP B 400
REMARK 465 PRO B 401
REMARK 465 ALA B 402
REMARK 465 ALA B 403
REMARK 465 SER B 404
REMARK 465 SER B 405
REMARK 465 SER B 406
REMARK 465 GLU B 407
REMARK 465 ARG B 408
REMARK 465 ASP B 634
REMARK 465 MET C -13
REMARK 465 GLY C -12
REMARK 465 GLY C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 GLY C -3
REMARK 465 MET C -2
REMARK 465 ALA C -1
REMARK 465 ASP C 400
REMARK 465 PRO C 401
REMARK 465 ALA C 402
REMARK 465 ALA C 403
REMARK 465 SER C 404
REMARK 465 SER C 405
REMARK 465 SER C 406
REMARK 465 GLU C 407
REMARK 465 ARG C 408
REMARK 465 ASP C 634
REMARK 465 THR H 28
REMARK 465 ILE H 223
REMARK 465 SER I 138
REMARK 465 ILE I 223
REMARK 465 ILE J 223
REMARK 465 CYS L 213
REMARK 465 CYS M 213
REMARK 465 CYS N 213
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 0 OG
REMARK 470 SER B 0 OG
REMARK 470 SER C 0 OG
REMARK 470 TYR H 27 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE H 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR H 30 OG1 CG2
REMARK 470 TYR H 31 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS H 65 CG CD CE NZ
REMARK 470 TYR I 27 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS I 65 CG CD CE NZ
REMARK 470 ASP I 136 CG OD1 OD2
REMARK 470 TYR J 27 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR J 28 OG1 CG2
REMARK 470 PHE J 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS J 65 CG CD CE NZ
REMARK 470 THR L 9 OG1 CG2
REMARK 470 THR M 9 OG1 CG2
REMARK 470 THR N 9 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CG2 VAL J 2 CB TYR J 27 1.82
REMARK 500 O SER J 140 CB SER J 191 1.83
REMARK 500 NZ LYS H 23 O SER H 76 1.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU C 576 CG GLU C 576 CD 0.092
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 15 -63.50 -144.86
REMARK 500 ARG A 87 9.21 59.91
REMARK 500 GLU A 168 101.43 -36.59
REMARK 500 ASN A 173 -73.10 -118.92
REMARK 500 ALA A 179 174.74 69.77
REMARK 500 ASP A 258 51.37 -115.75
REMARK 500 THR A 269 -82.60 -132.10
REMARK 500 ARG A 311 -137.88 45.99
REMARK 500 ARG A 316 68.74 61.99
REMARK 500 GLN A 325 -62.63 -130.49
REMARK 500 ASP A 337 23.88 -79.30
REMARK 500 SER A 340 85.63 -159.45
REMARK 500 SER A 424 -121.84 -137.46
REMARK 500 VAL A 466 -71.65 -117.65
REMARK 500 PRO A 532 130.70 -37.85
REMARK 500 ASP A 575 -176.34 -65.95
REMARK 500 ASN A 604 73.25 39.70
REMARK 500 ALA B 2 152.61 -43.27
REMARK 500 SER B 15 -61.68 -143.13
REMARK 500 ARG B 87 12.27 59.11
REMARK 500 SER B 115 7.45 -152.62
REMARK 500 GLU B 168 103.41 -35.89
REMARK 500 ASN B 173 -70.32 -118.45
REMARK 500 ALA B 179 174.69 69.74
REMARK 500 ASP B 258 51.95 -116.23
REMARK 500 THR B 269 -80.59 -130.93
REMARK 500 ARG B 311 -139.71 50.96
REMARK 500 ARG B 316 68.84 61.65
REMARK 500 GLN B 325 -61.93 -131.04
REMARK 500 ASP B 337 28.27 -79.92
REMARK 500 SER B 340 88.10 -159.16
REMARK 500 SER B 424 -121.03 -139.17
REMARK 500 VAL B 466 -71.84 -118.45
REMARK 500 PRO B 532 129.66 -39.85
REMARK 500 GLU B 576 -10.08 -44.83
REMARK 500 ASN B 604 72.72 35.80
REMARK 500 HIS B 632 0.69 -66.79
REMARK 500 SER C 15 -61.74 -145.11
REMARK 500 ARG C 87 11.69 58.92
REMARK 500 SER C 115 8.05 -150.53
REMARK 500 GLU C 168 104.08 -40.71
REMARK 500 ASN C 173 -71.63 -119.35
REMARK 500 ALA C 179 173.21 70.14
REMARK 500 ASP C 258 51.49 -117.57
REMARK 500 THR C 269 -81.81 -131.77
REMARK 500 ARG C 311 -137.02 48.20
REMARK 500 ARG C 316 67.95 63.49
REMARK 500 GLN C 325 -60.93 -131.82
REMARK 500 ASP C 337 23.91 -76.65
REMARK 500 SER C 340 86.52 -159.81
REMARK 500
REMARK 500 THIS ENTRY HAS 86 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY I 135 ASP I 136 138.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 635
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 636
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 635
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT UNIPROT ENTRY Q26966 HAS FOUR SEQUENCE ERRORS.
REMARK 999 THESE DISCREPANCIES HAVE BEEN REPEATEDLY INDICATED IN ALL PROVIOUS
REMARK 999 XRAY STRUCTURES RELATED TO TRYPANOSOMA CRUZI TRANS-SIALIDASE. THESE
REMARK 999 ERRORS CONCERN RESIDUES 262 (INDEED A THR), 476 (A HIS), 484 (A LEU)
REMARK 999 AND 558 (A VAL). HENCE, THESE DISCREPANCIES IN CHAINS A, B AND C,
REMARK 999 ARE NOT THE RESULT OF PROTEIN ENGINEERING.
DBREF 3OPZ A 1 634 UNP Q26966 Q26966_TRYCR 2 635
DBREF 3OPZ B 1 634 UNP Q26966 Q26966_TRYCR 2 635
DBREF 3OPZ C 1 634 UNP Q26966 Q26966_TRYCR 2 635
DBREF 3OPZ H 2 223 PDB 3OPZ 3OPZ 2 223
DBREF 3OPZ I 2 223 PDB 3OPZ 3OPZ 2 223
DBREF 3OPZ J 2 223 PDB 3OPZ 3OPZ 2 223
DBREF 3OPZ L 1 213 PDB 3OPZ 3OPZ 1 213
DBREF 3OPZ M 1 213 PDB 3OPZ 3OPZ 1 213
DBREF 3OPZ N 1 213 PDB 3OPZ 3OPZ 1 213
SEQADV 3OPZ MET A -13 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ GLY A -12 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ GLY A -11 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ SER A -10 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS A -9 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS A -8 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS A -7 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS A -6 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS A -5 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS A -4 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ GLY A -3 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ MET A -2 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ ALA A -1 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ SER A 0 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ PHE A 58 UNP Q26966 ASN 59 ENGINEERED MUTATION
SEQADV 3OPZ THR A 262 UNP Q26966 SER 263 SEE REMARK 999
SEQADV 3OPZ HIS A 476 UNP Q26966 ARG 477 SEE REMARK 999
SEQADV 3OPZ LEU A 484 UNP Q26966 VAL 485 SEE REMARK 999
SEQADV 3OPZ LYS A 495 UNP Q26966 SER 496 ENGINEERED MUTATION
SEQADV 3OPZ GLY A 496 UNP Q26966 VAL 497 ENGINEERED MUTATION
SEQADV 3OPZ LYS A 520 UNP Q26966 GLU 521 ENGINEERED MUTATION
SEQADV 3OPZ VAL A 558 UNP Q26966 GLU 559 SEE REMARK 999
SEQADV 3OPZ GLY A 593 UNP Q26966 ASP 594 ENGINEERED MUTATION
SEQADV 3OPZ ASP A 597 UNP Q26966 ILE 598 ENGINEERED MUTATION
SEQADV 3OPZ ARG A 599 UNP Q26966 HIS 600 ENGINEERED MUTATION
SEQADV 3OPZ MET B -13 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ GLY B -12 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ GLY B -11 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ SER B -10 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS B -9 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS B -8 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS B -7 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS B -6 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS B -5 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS B -4 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ GLY B -3 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ MET B -2 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ ALA B -1 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ SER B 0 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ PHE B 58 UNP Q26966 ASN 59 ENGINEERED MUTATION
SEQADV 3OPZ THR B 262 UNP Q26966 SER 263 ENGINEERED MUTATION
SEQADV 3OPZ HIS B 476 UNP Q26966 ARG 477 ENGINEERED MUTATION
SEQADV 3OPZ LEU B 484 UNP Q26966 VAL 485 ENGINEERED MUTATION
SEQADV 3OPZ LYS B 495 UNP Q26966 SER 496 ENGINEERED MUTATION
SEQADV 3OPZ GLY B 496 UNP Q26966 VAL 497 ENGINEERED MUTATION
SEQADV 3OPZ LYS B 520 UNP Q26966 GLU 521 ENGINEERED MUTATION
SEQADV 3OPZ VAL B 558 UNP Q26966 GLU 559 ENGINEERED MUTATION
SEQADV 3OPZ GLY B 593 UNP Q26966 ASP 594 ENGINEERED MUTATION
SEQADV 3OPZ ASP B 597 UNP Q26966 ILE 598 ENGINEERED MUTATION
SEQADV 3OPZ ARG B 599 UNP Q26966 HIS 600 ENGINEERED MUTATION
SEQADV 3OPZ MET C -13 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ GLY C -12 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ GLY C -11 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ SER C -10 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS C -9 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS C -8 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS C -7 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS C -6 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS C -5 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ HIS C -4 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ GLY C -3 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ MET C -2 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ ALA C -1 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ SER C 0 UNP Q26966 EXPRESSION TAG
SEQADV 3OPZ PHE C 58 UNP Q26966 ASN 59 ENGINEERED MUTATION
SEQADV 3OPZ THR C 262 UNP Q26966 SER 263 ENGINEERED MUTATION
SEQADV 3OPZ HIS C 476 UNP Q26966 ARG 477 ENGINEERED MUTATION
SEQADV 3OPZ LEU C 484 UNP Q26966 VAL 485 ENGINEERED MUTATION
SEQADV 3OPZ LYS C 495 UNP Q26966 SER 496 ENGINEERED MUTATION
SEQADV 3OPZ GLY C 496 UNP Q26966 VAL 497 ENGINEERED MUTATION
SEQADV 3OPZ LYS C 520 UNP Q26966 GLU 521 ENGINEERED MUTATION
SEQADV 3OPZ VAL C 558 UNP Q26966 GLU 559 ENGINEERED MUTATION
SEQADV 3OPZ GLY C 593 UNP Q26966 ASP 594 ENGINEERED MUTATION
SEQADV 3OPZ ASP C 597 UNP Q26966 ILE 598 ENGINEERED MUTATION
SEQADV 3OPZ ARG C 599 UNP Q26966 HIS 600 ENGINEERED MUTATION
SEQRES 1 A 648 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 A 648 SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU PHE LYS
SEQRES 3 A 648 ARG GLN SER SER LYS VAL PRO PHE GLU LYS ASP GLY LYS
SEQRES 4 A 648 VAL THR GLU ARG VAL VAL HIS SER PHE ARG LEU PRO ALA
SEQRES 5 A 648 LEU VAL ASN VAL ASP GLY VAL MET VAL ALA ILE ALA ASP
SEQRES 6 A 648 ALA ARG TYR GLU THR SER PHE ASP ASN SER LEU ILE ASP
SEQRES 7 A 648 THR VAL ALA LYS TYR SER VAL ASP ASP GLY GLU THR TRP
SEQRES 8 A 648 GLU THR GLN ILE ALA ILE LYS ASN SER ARG ALA SER SER
SEQRES 9 A 648 VAL SER ARG VAL VAL ASP PRO THR VAL ILE VAL LYS GLY
SEQRES 10 A 648 ASN LYS LEU TYR VAL LEU VAL GLY SER TYR ASN SER SER
SEQRES 11 A 648 ARG SER TYR TRP THR SER HIS GLY ASP ALA ARG ASP TRP
SEQRES 12 A 648 ASP ILE LEU LEU ALA VAL GLY GLU VAL THR LYS SER THR
SEQRES 13 A 648 ALA GLY GLY LYS ILE THR ALA SER ILE LYS TRP GLY SER
SEQRES 14 A 648 PRO VAL SER LEU LYS GLU PHE PHE PRO ALA GLU MET GLU
SEQRES 15 A 648 GLY MET HIS THR ASN GLN PHE LEU GLY GLY ALA GLY VAL
SEQRES 16 A 648 ALA ILE VAL ALA SER ASN GLY ASN LEU VAL TYR PRO VAL
SEQRES 17 A 648 GLN VAL THR ASN LYS LYS LYS GLN VAL PHE SER LYS ILE
SEQRES 18 A 648 PHE TYR SER GLU ASP GLU GLY LYS THR TRP LYS PHE GLY
SEQRES 19 A 648 LYS GLY ARG SER ALA PHE GLY CYS SER GLU PRO VAL ALA
SEQRES 20 A 648 LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN THR ARG VAL
SEQRES 21 A 648 ASP TYR ARG ARG ARG LEU VAL TYR GLU SER SER ASP MET
SEQRES 22 A 648 GLY ASN THR TRP LEU GLU ALA VAL GLY THR LEU SER ARG
SEQRES 23 A 648 VAL TRP GLY PRO SER PRO LYS SER ASN GLN PRO GLY SER
SEQRES 24 A 648 GLN SER SER PHE THR ALA VAL THR ILE GLU GLY MET ARG
SEQRES 25 A 648 VAL MET LEU PHE THR HIS PRO LEU ASN PHE LYS GLY ARG
SEQRES 26 A 648 TRP LEU ARG ASP ARG LEU ASN LEU TRP LEU THR ASP ASN
SEQRES 27 A 648 GLN ARG ILE TYR ASN VAL GLY GLN VAL SER ILE GLY ASP
SEQRES 28 A 648 GLU ASN SER ALA TYR SER SER VAL LEU TYR LYS ASP ASP
SEQRES 29 A 648 LYS LEU TYR CYS LEU HIS GLU ILE ASN SER ASN GLU VAL
SEQRES 30 A 648 TYR SER LEU VAL PHE ALA ARG LEU VAL GLY GLU LEU ARG
SEQRES 31 A 648 ILE ILE LYS SER VAL LEU GLN SER TRP LYS ASN TRP ASP
SEQRES 32 A 648 SER HIS LEU SER SER ILE CYS THR PRO ALA ASP PRO ALA
SEQRES 33 A 648 ALA SER SER SER GLU ARG GLY CYS GLY PRO ALA VAL THR
SEQRES 34 A 648 THR VAL GLY LEU VAL GLY PHE LEU SER HIS SER ALA THR
SEQRES 35 A 648 LYS THR GLU TRP GLU ASP ALA TYR ARG CYS VAL ASN ALA
SEQRES 36 A 648 SER THR ALA ASN ALA GLU ARG VAL PRO ASN GLY LEU LYS
SEQRES 37 A 648 PHE ALA GLY VAL GLY GLY GLY ALA LEU TRP PRO VAL SER
SEQRES 38 A 648 GLN GLN GLY GLN ASN GLN ARG TYR HIS PHE ALA ASN HIS
SEQRES 39 A 648 ALA PHE THR LEU VAL ALA SER VAL THR ILE HIS GLU VAL
SEQRES 40 A 648 PRO LYS GLY ALA SER PRO LEU LEU GLY ALA SER LEU ASP
SEQRES 41 A 648 SER SER GLY GLY LYS LYS LEU LEU GLY LEU SER TYR ASP
SEQRES 42 A 648 LYS ARG HIS GLN TRP GLN PRO ILE TYR GLY SER THR PRO
SEQRES 43 A 648 VAL THR PRO THR GLY SER TRP GLU MET GLY LYS ARG TYR
SEQRES 44 A 648 HIS VAL VAL LEU THR MET ALA ASN LYS ILE GLY SER VAL
SEQRES 45 A 648 TYR ILE ASP GLY GLU PRO LEU GLU GLY SER GLY GLN THR
SEQRES 46 A 648 VAL VAL PRO ASP GLU ARG THR PRO ASP ILE SER HIS PHE
SEQRES 47 A 648 TYR VAL GLY GLY TYR LYS ARG SER GLY MET PRO THR ASP
SEQRES 48 A 648 SER ARG VAL THR VAL ASN ASN VAL LEU LEU TYR ASN ARG
SEQRES 49 A 648 GLN LEU ASN ALA GLU GLU ILE ARG THR LEU PHE LEU SER
SEQRES 50 A 648 GLN ASP LEU ILE GLY THR GLU ALA HIS MET ASP
SEQRES 1 B 648 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 B 648 SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU PHE LYS
SEQRES 3 B 648 ARG GLN SER SER LYS VAL PRO PHE GLU LYS ASP GLY LYS
SEQRES 4 B 648 VAL THR GLU ARG VAL VAL HIS SER PHE ARG LEU PRO ALA
SEQRES 5 B 648 LEU VAL ASN VAL ASP GLY VAL MET VAL ALA ILE ALA ASP
SEQRES 6 B 648 ALA ARG TYR GLU THR SER PHE ASP ASN SER LEU ILE ASP
SEQRES 7 B 648 THR VAL ALA LYS TYR SER VAL ASP ASP GLY GLU THR TRP
SEQRES 8 B 648 GLU THR GLN ILE ALA ILE LYS ASN SER ARG ALA SER SER
SEQRES 9 B 648 VAL SER ARG VAL VAL ASP PRO THR VAL ILE VAL LYS GLY
SEQRES 10 B 648 ASN LYS LEU TYR VAL LEU VAL GLY SER TYR ASN SER SER
SEQRES 11 B 648 ARG SER TYR TRP THR SER HIS GLY ASP ALA ARG ASP TRP
SEQRES 12 B 648 ASP ILE LEU LEU ALA VAL GLY GLU VAL THR LYS SER THR
SEQRES 13 B 648 ALA GLY GLY LYS ILE THR ALA SER ILE LYS TRP GLY SER
SEQRES 14 B 648 PRO VAL SER LEU LYS GLU PHE PHE PRO ALA GLU MET GLU
SEQRES 15 B 648 GLY MET HIS THR ASN GLN PHE LEU GLY GLY ALA GLY VAL
SEQRES 16 B 648 ALA ILE VAL ALA SER ASN GLY ASN LEU VAL TYR PRO VAL
SEQRES 17 B 648 GLN VAL THR ASN LYS LYS LYS GLN VAL PHE SER LYS ILE
SEQRES 18 B 648 PHE TYR SER GLU ASP GLU GLY LYS THR TRP LYS PHE GLY
SEQRES 19 B 648 LYS GLY ARG SER ALA PHE GLY CYS SER GLU PRO VAL ALA
SEQRES 20 B 648 LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN THR ARG VAL
SEQRES 21 B 648 ASP TYR ARG ARG ARG LEU VAL TYR GLU SER SER ASP MET
SEQRES 22 B 648 GLY ASN THR TRP LEU GLU ALA VAL GLY THR LEU SER ARG
SEQRES 23 B 648 VAL TRP GLY PRO SER PRO LYS SER ASN GLN PRO GLY SER
SEQRES 24 B 648 GLN SER SER PHE THR ALA VAL THR ILE GLU GLY MET ARG
SEQRES 25 B 648 VAL MET LEU PHE THR HIS PRO LEU ASN PHE LYS GLY ARG
SEQRES 26 B 648 TRP LEU ARG ASP ARG LEU ASN LEU TRP LEU THR ASP ASN
SEQRES 27 B 648 GLN ARG ILE TYR ASN VAL GLY GLN VAL SER ILE GLY ASP
SEQRES 28 B 648 GLU ASN SER ALA TYR SER SER VAL LEU TYR LYS ASP ASP
SEQRES 29 B 648 LYS LEU TYR CYS LEU HIS GLU ILE ASN SER ASN GLU VAL
SEQRES 30 B 648 TYR SER LEU VAL PHE ALA ARG LEU VAL GLY GLU LEU ARG
SEQRES 31 B 648 ILE ILE LYS SER VAL LEU GLN SER TRP LYS ASN TRP ASP
SEQRES 32 B 648 SER HIS LEU SER SER ILE CYS THR PRO ALA ASP PRO ALA
SEQRES 33 B 648 ALA SER SER SER GLU ARG GLY CYS GLY PRO ALA VAL THR
SEQRES 34 B 648 THR VAL GLY LEU VAL GLY PHE LEU SER HIS SER ALA THR
SEQRES 35 B 648 LYS THR GLU TRP GLU ASP ALA TYR ARG CYS VAL ASN ALA
SEQRES 36 B 648 SER THR ALA ASN ALA GLU ARG VAL PRO ASN GLY LEU LYS
SEQRES 37 B 648 PHE ALA GLY VAL GLY GLY GLY ALA LEU TRP PRO VAL SER
SEQRES 38 B 648 GLN GLN GLY GLN ASN GLN ARG TYR HIS PHE ALA ASN HIS
SEQRES 39 B 648 ALA PHE THR LEU VAL ALA SER VAL THR ILE HIS GLU VAL
SEQRES 40 B 648 PRO LYS GLY ALA SER PRO LEU LEU GLY ALA SER LEU ASP
SEQRES 41 B 648 SER SER GLY GLY LYS LYS LEU LEU GLY LEU SER TYR ASP
SEQRES 42 B 648 LYS ARG HIS GLN TRP GLN PRO ILE TYR GLY SER THR PRO
SEQRES 43 B 648 VAL THR PRO THR GLY SER TRP GLU MET GLY LYS ARG TYR
SEQRES 44 B 648 HIS VAL VAL LEU THR MET ALA ASN LYS ILE GLY SER VAL
SEQRES 45 B 648 TYR ILE ASP GLY GLU PRO LEU GLU GLY SER GLY GLN THR
SEQRES 46 B 648 VAL VAL PRO ASP GLU ARG THR PRO ASP ILE SER HIS PHE
SEQRES 47 B 648 TYR VAL GLY GLY TYR LYS ARG SER GLY MET PRO THR ASP
SEQRES 48 B 648 SER ARG VAL THR VAL ASN ASN VAL LEU LEU TYR ASN ARG
SEQRES 49 B 648 GLN LEU ASN ALA GLU GLU ILE ARG THR LEU PHE LEU SER
SEQRES 50 B 648 GLN ASP LEU ILE GLY THR GLU ALA HIS MET ASP
SEQRES 1 C 648 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 C 648 SER LEU ALA PRO GLY SER SER ARG VAL GLU LEU PHE LYS
SEQRES 3 C 648 ARG GLN SER SER LYS VAL PRO PHE GLU LYS ASP GLY LYS
SEQRES 4 C 648 VAL THR GLU ARG VAL VAL HIS SER PHE ARG LEU PRO ALA
SEQRES 5 C 648 LEU VAL ASN VAL ASP GLY VAL MET VAL ALA ILE ALA ASP
SEQRES 6 C 648 ALA ARG TYR GLU THR SER PHE ASP ASN SER LEU ILE ASP
SEQRES 7 C 648 THR VAL ALA LYS TYR SER VAL ASP ASP GLY GLU THR TRP
SEQRES 8 C 648 GLU THR GLN ILE ALA ILE LYS ASN SER ARG ALA SER SER
SEQRES 9 C 648 VAL SER ARG VAL VAL ASP PRO THR VAL ILE VAL LYS GLY
SEQRES 10 C 648 ASN LYS LEU TYR VAL LEU VAL GLY SER TYR ASN SER SER
SEQRES 11 C 648 ARG SER TYR TRP THR SER HIS GLY ASP ALA ARG ASP TRP
SEQRES 12 C 648 ASP ILE LEU LEU ALA VAL GLY GLU VAL THR LYS SER THR
SEQRES 13 C 648 ALA GLY GLY LYS ILE THR ALA SER ILE LYS TRP GLY SER
SEQRES 14 C 648 PRO VAL SER LEU LYS GLU PHE PHE PRO ALA GLU MET GLU
SEQRES 15 C 648 GLY MET HIS THR ASN GLN PHE LEU GLY GLY ALA GLY VAL
SEQRES 16 C 648 ALA ILE VAL ALA SER ASN GLY ASN LEU VAL TYR PRO VAL
SEQRES 17 C 648 GLN VAL THR ASN LYS LYS LYS GLN VAL PHE SER LYS ILE
SEQRES 18 C 648 PHE TYR SER GLU ASP GLU GLY LYS THR TRP LYS PHE GLY
SEQRES 19 C 648 LYS GLY ARG SER ALA PHE GLY CYS SER GLU PRO VAL ALA
SEQRES 20 C 648 LEU GLU TRP GLU GLY LYS LEU ILE ILE ASN THR ARG VAL
SEQRES 21 C 648 ASP TYR ARG ARG ARG LEU VAL TYR GLU SER SER ASP MET
SEQRES 22 C 648 GLY ASN THR TRP LEU GLU ALA VAL GLY THR LEU SER ARG
SEQRES 23 C 648 VAL TRP GLY PRO SER PRO LYS SER ASN GLN PRO GLY SER
SEQRES 24 C 648 GLN SER SER PHE THR ALA VAL THR ILE GLU GLY MET ARG
SEQRES 25 C 648 VAL MET LEU PHE THR HIS PRO LEU ASN PHE LYS GLY ARG
SEQRES 26 C 648 TRP LEU ARG ASP ARG LEU ASN LEU TRP LEU THR ASP ASN
SEQRES 27 C 648 GLN ARG ILE TYR ASN VAL GLY GLN VAL SER ILE GLY ASP
SEQRES 28 C 648 GLU ASN SER ALA TYR SER SER VAL LEU TYR LYS ASP ASP
SEQRES 29 C 648 LYS LEU TYR CYS LEU HIS GLU ILE ASN SER ASN GLU VAL
SEQRES 30 C 648 TYR SER LEU VAL PHE ALA ARG LEU VAL GLY GLU LEU ARG
SEQRES 31 C 648 ILE ILE LYS SER VAL LEU GLN SER TRP LYS ASN TRP ASP
SEQRES 32 C 648 SER HIS LEU SER SER ILE CYS THR PRO ALA ASP PRO ALA
SEQRES 33 C 648 ALA SER SER SER GLU ARG GLY CYS GLY PRO ALA VAL THR
SEQRES 34 C 648 THR VAL GLY LEU VAL GLY PHE LEU SER HIS SER ALA THR
SEQRES 35 C 648 LYS THR GLU TRP GLU ASP ALA TYR ARG CYS VAL ASN ALA
SEQRES 36 C 648 SER THR ALA ASN ALA GLU ARG VAL PRO ASN GLY LEU LYS
SEQRES 37 C 648 PHE ALA GLY VAL GLY GLY GLY ALA LEU TRP PRO VAL SER
SEQRES 38 C 648 GLN GLN GLY GLN ASN GLN ARG TYR HIS PHE ALA ASN HIS
SEQRES 39 C 648 ALA PHE THR LEU VAL ALA SER VAL THR ILE HIS GLU VAL
SEQRES 40 C 648 PRO LYS GLY ALA SER PRO LEU LEU GLY ALA SER LEU ASP
SEQRES 41 C 648 SER SER GLY GLY LYS LYS LEU LEU GLY LEU SER TYR ASP
SEQRES 42 C 648 LYS ARG HIS GLN TRP GLN PRO ILE TYR GLY SER THR PRO
SEQRES 43 C 648 VAL THR PRO THR GLY SER TRP GLU MET GLY LYS ARG TYR
SEQRES 44 C 648 HIS VAL VAL LEU THR MET ALA ASN LYS ILE GLY SER VAL
SEQRES 45 C 648 TYR ILE ASP GLY GLU PRO LEU GLU GLY SER GLY GLN THR
SEQRES 46 C 648 VAL VAL PRO ASP GLU ARG THR PRO ASP ILE SER HIS PHE
SEQRES 47 C 648 TYR VAL GLY GLY TYR LYS ARG SER GLY MET PRO THR ASP
SEQRES 48 C 648 SER ARG VAL THR VAL ASN ASN VAL LEU LEU TYR ASN ARG
SEQRES 49 C 648 GLN LEU ASN ALA GLU GLU ILE ARG THR LEU PHE LEU SER
SEQRES 50 C 648 GLN ASP LEU ILE GLY THR GLU ALA HIS MET ASP
SEQRES 1 H 222 VAL LYS LEU GLN GLN SER GLY VAL GLU LEU VAL ARG PRO
SEQRES 2 H 222 GLY THR SER VAL LYS MET SER CYS LYS ALA VAL GLY TYR
SEQRES 3 H 222 THR PHE THR TYR ASP TRP ILE GLY TRP VAL LYS GLN ARG
SEQRES 4 H 222 PRO GLY HIS GLY LEU GLU TRP ILE GLY ASP ILE TYR LEU
SEQRES 5 H 222 GLY GLY GLY TYR ILE ASN TYR ASN GLU LYS PHE LYS GLY
SEQRES 6 H 222 LYS VAL ILE LEU THR ALA ASP THR SER SER SER THR ALA
SEQRES 7 H 222 TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER ALA
SEQRES 8 H 222 ILE TYR TYR CYS ALA ARG GLY HIS TYR ASP GLY SER TYR
SEQRES 9 H 222 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER
SEQRES 10 H 222 SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA
SEQRES 11 H 222 PRO VAL CYS GLY ASP THR SER GLY SER SER VAL THR LEU
SEQRES 12 H 222 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 H 222 LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 H 222 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 H 222 SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER
SEQRES 16 H 222 GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 H 222 THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO THR
SEQRES 18 H 222 ILE
SEQRES 1 I 222 VAL LYS LEU GLN GLN SER GLY VAL GLU LEU VAL ARG PRO
SEQRES 2 I 222 GLY THR SER VAL LYS MET SER CYS LYS ALA VAL GLY TYR
SEQRES 3 I 222 THR PHE THR TYR ASP TRP ILE GLY TRP VAL LYS GLN ARG
SEQRES 4 I 222 PRO GLY HIS GLY LEU GLU TRP ILE GLY ASP ILE TYR LEU
SEQRES 5 I 222 GLY GLY GLY TYR ILE ASN TYR ASN GLU LYS PHE LYS GLY
SEQRES 6 I 222 LYS VAL ILE LEU THR ALA ASP THR SER SER SER THR ALA
SEQRES 7 I 222 TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER ALA
SEQRES 8 I 222 ILE TYR TYR CYS ALA ARG GLY HIS TYR ASP GLY SER TYR
SEQRES 9 I 222 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER
SEQRES 10 I 222 SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA
SEQRES 11 I 222 PRO VAL CYS GLY ASP THR SER GLY SER SER VAL THR LEU
SEQRES 12 I 222 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 I 222 LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 I 222 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 I 222 SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER
SEQRES 16 I 222 GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 I 222 THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO THR
SEQRES 18 I 222 ILE
SEQRES 1 J 222 VAL LYS LEU GLN GLN SER GLY VAL GLU LEU VAL ARG PRO
SEQRES 2 J 222 GLY THR SER VAL LYS MET SER CYS LYS ALA VAL GLY TYR
SEQRES 3 J 222 THR PHE THR TYR ASP TRP ILE GLY TRP VAL LYS GLN ARG
SEQRES 4 J 222 PRO GLY HIS GLY LEU GLU TRP ILE GLY ASP ILE TYR LEU
SEQRES 5 J 222 GLY GLY GLY TYR ILE ASN TYR ASN GLU LYS PHE LYS GLY
SEQRES 6 J 222 LYS VAL ILE LEU THR ALA ASP THR SER SER SER THR ALA
SEQRES 7 J 222 TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER ALA
SEQRES 8 J 222 ILE TYR TYR CYS ALA ARG GLY HIS TYR ASP GLY SER TYR
SEQRES 9 J 222 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER
SEQRES 10 J 222 SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA
SEQRES 11 J 222 PRO VAL CYS GLY ASP THR SER GLY SER SER VAL THR LEU
SEQRES 12 J 222 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 J 222 LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 J 222 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 J 222 SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER
SEQRES 16 J 222 GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 J 222 THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO THR
SEQRES 18 J 222 ILE
SEQRES 1 L 213 ASP VAL LEU MET THR GLN THR PRO THR ILE MET SER ALA
SEQRES 2 L 213 SER ILE GLY GLU GLU ILE THR LEU THR CYS SER ALA SER
SEQRES 3 L 213 SER SER VAL SER HIS MET HIS TRP TYR GLN HIS LYS SER
SEQRES 4 L 213 GLY THR SER PRO LYS LEU LEU ILE TYR ILE THR SER TYR
SEQRES 5 L 213 LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SER GLY
SEQRES 6 L 213 SER GLY THR PHE TYR SER LEU THR ILE SER SER VAL GLU
SEQRES 7 L 213 ALA GLU ASP ALA ALA ASP TYR TYR CYS HIS GLN TRP SER
SEQRES 8 L 213 THR PHE PRO SER THR PHE GLY SER GLY THR LYS LEU GLU
SEQRES 9 L 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 L 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 L 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 L 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 L 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 L 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 L 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 L 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 L 213 ASN ARG ASN GLU CYS
SEQRES 1 M 213 ASP VAL LEU MET THR GLN THR PRO THR ILE MET SER ALA
SEQRES 2 M 213 SER ILE GLY GLU GLU ILE THR LEU THR CYS SER ALA SER
SEQRES 3 M 213 SER SER VAL SER HIS MET HIS TRP TYR GLN HIS LYS SER
SEQRES 4 M 213 GLY THR SER PRO LYS LEU LEU ILE TYR ILE THR SER TYR
SEQRES 5 M 213 LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SER GLY
SEQRES 6 M 213 SER GLY THR PHE TYR SER LEU THR ILE SER SER VAL GLU
SEQRES 7 M 213 ALA GLU ASP ALA ALA ASP TYR TYR CYS HIS GLN TRP SER
SEQRES 8 M 213 THR PHE PRO SER THR PHE GLY SER GLY THR LYS LEU GLU
SEQRES 9 M 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 M 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 M 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 M 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 M 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 M 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 M 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 M 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 M 213 ASN ARG ASN GLU CYS
SEQRES 1 N 213 ASP VAL LEU MET THR GLN THR PRO THR ILE MET SER ALA
SEQRES 2 N 213 SER ILE GLY GLU GLU ILE THR LEU THR CYS SER ALA SER
SEQRES 3 N 213 SER SER VAL SER HIS MET HIS TRP TYR GLN HIS LYS SER
SEQRES 4 N 213 GLY THR SER PRO LYS LEU LEU ILE TYR ILE THR SER TYR
SEQRES 5 N 213 LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SER GLY
SEQRES 6 N 213 SER GLY THR PHE TYR SER LEU THR ILE SER SER VAL GLU
SEQRES 7 N 213 ALA GLU ASP ALA ALA ASP TYR TYR CYS HIS GLN TRP SER
SEQRES 8 N 213 THR PHE PRO SER THR PHE GLY SER GLY THR LYS LEU GLU
SEQRES 9 N 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 N 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 N 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 N 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 N 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 N 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 N 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 N 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 N 213 ASN ARG ASN GLU CYS
HET NA A 635 1
HET DIO A 636 6
HET DIO B 635 6
HETNAM NA SODIUM ION
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
FORMUL 10 NA NA 1+
FORMUL 11 DIO 2(C4 H8 O2)
FORMUL 13 HOH *42(H2 O)
HELIX 1 1 TYR A 119 HIS A 123 5 5
HELIX 2 2 LYS A 160 PHE A 163 5 4
HELIX 3 3 LEU A 371 ILE A 395 1 25
HELIX 4 4 GLN A 473 HIS A 480 5 8
HELIX 5 5 ASN A 613 SER A 623 1 11
HELIX 6 6 TYR B 119 HIS B 123 5 5
HELIX 7 7 LYS B 160 PHE B 163 5 4
HELIX 8 8 LEU B 371 SER B 394 1 24
HELIX 9 9 GLN B 473 HIS B 480 5 8
HELIX 10 10 ASN B 613 SER B 623 1 11
HELIX 11 11 TYR C 119 HIS C 123 5 5
HELIX 12 12 LYS C 160 PHE C 163 5 4
HELIX 13 13 LEU C 371 SER C 394 1 24
HELIX 14 14 GLN C 473 HIS C 480 5 8
HELIX 15 15 ASN C 613 SER C 623 1 11
HELIX 16 16 GLU H 62 LYS H 65 5 4
HELIX 17 17 THR H 87 SER H 91 5 5
HELIX 18 18 SER H 162 SER H 164 5 3
HELIX 19 19 THR H 190 TRP H 194 5 5
HELIX 20 20 PRO H 206 SER H 209 5 4
HELIX 21 21 GLU I 62 LYS I 65 5 4
HELIX 22 22 THR I 87 SER I 91 5 5
HELIX 23 23 SER I 162 SER I 164 5 3
HELIX 24 24 SER I 192 TRP I 194 5 3
HELIX 25 25 GLU J 62 LYS J 65 5 4
HELIX 26 26 THR J 87 SER J 91 5 5
HELIX 27 27 SER J 162 SER J 164 5 3
HELIX 28 28 SER J 192 TRP J 194 5 3
HELIX 29 29 ILE L 49 SER L 51 5 3
HELIX 30 30 GLU L 78 ALA L 82 5 5
HELIX 31 31 SER L 120 SER L 126 1 7
HELIX 32 32 LYS L 182 ARG L 187 1 6
HELIX 33 33 GLU M 78 ALA M 82 5 5
HELIX 34 34 SER M 120 SER M 126 1 7
HELIX 35 35 LYS M 182 ARG M 187 1 6
HELIX 36 36 GLU N 78 ALA N 82 5 5
HELIX 37 37 SER N 120 SER N 126 1 7
HELIX 38 38 LYS N 182 ARG N 187 1 6
SHEET 1 A 4 SER A 6 PHE A 11 0
SHEET 2 A 4 VAL A 363 ARG A 370 -1 O ARG A 370 N SER A 6
SHEET 3 A 4 LYS A 351 SER A 360 -1 N CYS A 354 O ALA A 369
SHEET 4 A 4 SER A 343 LYS A 348 -1 N LEU A 346 O TYR A 353
SHEET 1 B 2 LYS A 17 LYS A 22 0
SHEET 2 B 2 LYS A 25 VAL A 30 -1 O THR A 27 N PHE A 20
SHEET 1 C 4 SER A 33 VAL A 42 0
SHEET 2 C 4 VAL A 45 ARG A 53 -1 O ASP A 51 N ARG A 35
SHEET 3 C 4 ILE A 63 SER A 70 -1 O ASP A 64 N ALA A 52
SHEET 4 C 4 GLU A 78 ILE A 83 -1 O GLN A 80 N ALA A 67
SHEET 1 D 3 LYS A 146 TRP A 153 0
SHEET 2 D 3 TRP A 129 ALA A 143 -1 N ALA A 143 O LYS A 146
SHEET 3 D 3 VAL A 157 SER A 158 -1 O VAL A 157 N LEU A 133
SHEET 1 E 5 LYS A 146 TRP A 153 0
SHEET 2 E 5 TRP A 129 ALA A 143 -1 N ALA A 143 O LYS A 146
SHEET 3 E 5 LYS A 105 TYR A 113 -1 N VAL A 110 O LEU A 132
SHEET 4 E 5 ARG A 93 LYS A 102 -1 N ILE A 100 O TYR A 107
SHEET 5 E 5 GLY A 180 VAL A 181 1 O GLY A 180 N VAL A 99
SHEET 1 F 4 GLU A 166 MET A 167 0
SHEET 2 F 4 MET A 170 GLY A 177 -1 O MET A 170 N MET A 167
SHEET 3 F 4 LEU A 190 ASN A 198 -1 O GLN A 195 N LEU A 176
SHEET 4 F 4 ILE A 183 VAL A 184 -1 N ILE A 183 O VAL A 191
SHEET 1 G 5 GLU A 166 MET A 167 0
SHEET 2 G 5 MET A 170 GLY A 177 -1 O MET A 170 N MET A 167
SHEET 3 G 5 LEU A 190 ASN A 198 -1 O GLN A 195 N LEU A 176
SHEET 4 G 5 VAL A 203 SER A 210 -1 O PHE A 204 N VAL A 196
SHEET 5 G 5 LYS A 218 PHE A 219 -1 O LYS A 218 N TYR A 209
SHEET 1 H 4 CYS A 228 TRP A 236 0
SHEET 2 H 4 LYS A 239 VAL A 246 -1 O ARG A 245 N SER A 229
SHEET 3 H 4 VAL A 253 SER A 256 -1 O TYR A 254 N ILE A 242
SHEET 4 H 4 LEU A 264 GLU A 265 -1 O LEU A 264 N GLU A 255
SHEET 1 I 4 PHE A 289 ILE A 294 0
SHEET 2 I 4 MET A 297 PRO A 305 -1 O VAL A 299 N VAL A 292
SHEET 3 I 4 LEU A 317 THR A 322 -1 O TRP A 320 N PHE A 302
SHEET 4 I 4 ILE A 327 GLN A 332 -1 O TYR A 328 N LEU A 321
SHEET 1 J 7 ALA A 446 VAL A 449 0
SHEET 2 J 7 GLY A 452 PHE A 455 -1 O LYS A 454 N GLU A 447
SHEET 3 J 7 VAL A 600 TYR A 608 -1 O VAL A 600 N PHE A 455
SHEET 4 J 7 PHE A 482 ILE A 490 -1 N THR A 483 O TYR A 608
SHEET 5 J 7 ARG A 544 ALA A 552 -1 O TYR A 545 N VAL A 488
SHEET 6 J 7 ILE A 555 ILE A 560 -1 O SER A 557 N THR A 550
SHEET 7 J 7 GLU A 563 PRO A 564 -1 O GLU A 563 N ILE A 560
SHEET 1 K13 TRP A 524 TYR A 528 0
SHEET 2 K13 LYS A 512 ASP A 519 -1 N GLY A 515 O ILE A 527
SHEET 3 K13 ALA A 497 SER A 504 -1 N LEU A 501 O LEU A 516
SHEET 4 K13 HIS A 583 VAL A 586 -1 O HIS A 583 N SER A 504
SHEET 5 K13 GLY A 461 PRO A 465 -1 N TRP A 464 O PHE A 584
SHEET 6 K13 ALA A 441 ALA A 444 -1 N SER A 442 O LEU A 463
SHEET 7 K13 GLU A 431 ASP A 434 -1 N TRP A 432 O ALA A 441
SHEET 8 K13 LEU A 419 ALA A 427 -1 N SER A 426 O GLU A 433
SHEET 9 K13 VAL A 600 TYR A 608 -1 O VAL A 605 N LEU A 423
SHEET 10 K13 PHE A 482 ILE A 490 -1 N THR A 483 O TYR A 608
SHEET 11 K13 ARG A 544 ALA A 552 -1 O TYR A 545 N VAL A 488
SHEET 12 K13 ILE A 555 ILE A 560 -1 O SER A 557 N THR A 550
SHEET 13 K13 GLN A 570 THR A 571 -1 O GLN A 570 N GLY A 556
SHEET 1 L 4 SER B 6 PHE B 11 0
SHEET 2 L 4 VAL B 363 ARG B 370 -1 O ARG B 370 N SER B 6
SHEET 3 L 4 LYS B 351 SER B 360 -1 N CYS B 354 O ALA B 369
SHEET 4 L 4 SER B 343 LYS B 348 -1 N SER B 344 O LEU B 355
SHEET 1 M 2 LYS B 17 LYS B 22 0
SHEET 2 M 2 LYS B 25 VAL B 30 -1 O THR B 27 N PHE B 20
SHEET 1 N 4 SER B 33 VAL B 42 0
SHEET 2 N 4 VAL B 45 ARG B 53 -1 O VAL B 47 N VAL B 40
SHEET 3 N 4 ILE B 63 SER B 70 -1 O LYS B 68 N ALA B 48
SHEET 4 N 4 GLU B 78 ILE B 83 -1 O ALA B 82 N THR B 65
SHEET 1 O 3 LYS B 146 TRP B 153 0
SHEET 2 O 3 TRP B 129 ALA B 143 -1 N ALA B 143 O LYS B 146
SHEET 3 O 3 VAL B 157 SER B 158 -1 O VAL B 157 N LEU B 133
SHEET 1 P 5 LYS B 146 TRP B 153 0
SHEET 2 P 5 TRP B 129 ALA B 143 -1 N ALA B 143 O LYS B 146
SHEET 3 P 5 LYS B 105 TYR B 113 -1 N VAL B 110 O LEU B 132
SHEET 4 P 5 ARG B 93 LYS B 102 -1 N ILE B 100 O TYR B 107
SHEET 5 P 5 GLY B 180 VAL B 181 1 O GLY B 180 N VAL B 99
SHEET 1 Q 4 GLU B 166 MET B 167 0
SHEET 2 Q 4 MET B 170 GLY B 177 -1 O MET B 170 N MET B 167
SHEET 3 Q 4 LEU B 190 ASN B 198 -1 O GLN B 195 N LEU B 176
SHEET 4 Q 4 ILE B 183 VAL B 184 -1 N ILE B 183 O VAL B 191
SHEET 1 R 5 GLU B 166 MET B 167 0
SHEET 2 R 5 MET B 170 GLY B 177 -1 O MET B 170 N MET B 167
SHEET 3 R 5 LEU B 190 ASN B 198 -1 O GLN B 195 N LEU B 176
SHEET 4 R 5 VAL B 203 SER B 210 -1 O PHE B 204 N VAL B 196
SHEET 5 R 5 LYS B 218 PHE B 219 -1 O LYS B 218 N TYR B 209
SHEET 1 S 4 SER B 229 TRP B 236 0
SHEET 2 S 4 LYS B 239 ARG B 245 -1 O ARG B 245 N SER B 229
SHEET 3 S 4 VAL B 253 SER B 256 -1 O TYR B 254 N ILE B 242
SHEET 4 S 4 LEU B 264 GLU B 265 -1 O LEU B 264 N GLU B 255
SHEET 1 T 4 PHE B 289 ILE B 294 0
SHEET 2 T 4 MET B 297 PRO B 305 -1 O VAL B 299 N VAL B 292
SHEET 3 T 4 LEU B 317 THR B 322 -1 O TRP B 320 N PHE B 302
SHEET 4 T 4 ILE B 327 GLN B 332 -1 O TYR B 328 N LEU B 321
SHEET 1 U 7 ALA B 446 VAL B 449 0
SHEET 2 U 7 GLY B 452 PHE B 455 -1 O LYS B 454 N GLU B 447
SHEET 3 U 7 VAL B 600 TYR B 608 -1 O VAL B 600 N PHE B 455
SHEET 4 U 7 PHE B 482 ILE B 490 -1 N VAL B 485 O LEU B 606
SHEET 5 U 7 ARG B 544 ALA B 552 -1 O TYR B 545 N VAL B 488
SHEET 6 U 7 ILE B 555 ILE B 560 -1 O SER B 557 N THR B 550
SHEET 7 U 7 GLU B 563 PRO B 564 -1 O GLU B 563 N ILE B 560
SHEET 1 V13 TRP B 524 TYR B 528 0
SHEET 2 V13 LYS B 512 ASP B 519 -1 N GLY B 515 O ILE B 527
SHEET 3 V13 ALA B 497 SER B 504 -1 N LEU B 501 O LEU B 516
SHEET 4 V13 HIS B 583 VAL B 586 -1 O HIS B 583 N SER B 504
SHEET 5 V13 GLY B 461 PRO B 465 -1 N TRP B 464 O PHE B 584
SHEET 6 V13 ALA B 441 ALA B 444 -1 N SER B 442 O LEU B 463
SHEET 7 V13 GLU B 431 ASP B 434 -1 N TRP B 432 O ALA B 441
SHEET 8 V13 LEU B 419 ALA B 427 -1 N SER B 426 O GLU B 433
SHEET 9 V13 VAL B 600 TYR B 608 -1 O VAL B 605 N LEU B 423
SHEET 10 V13 PHE B 482 ILE B 490 -1 N VAL B 485 O LEU B 606
SHEET 11 V13 ARG B 544 ALA B 552 -1 O TYR B 545 N VAL B 488
SHEET 12 V13 ILE B 555 ILE B 560 -1 O SER B 557 N THR B 550
SHEET 13 V13 GLN B 570 THR B 571 -1 O GLN B 570 N GLY B 556
SHEET 1 W 4 SER C 6 PHE C 11 0
SHEET 2 W 4 VAL C 363 ARG C 370 -1 O ARG C 370 N SER C 6
SHEET 3 W 4 LYS C 351 SER C 360 -1 N CYS C 354 O ALA C 369
SHEET 4 W 4 SER C 343 LYS C 348 -1 N LEU C 346 O TYR C 353
SHEET 1 X 2 LYS C 17 LYS C 22 0
SHEET 2 X 2 LYS C 25 VAL C 30 -1 O THR C 27 N PHE C 20
SHEET 1 Y 4 SER C 33 VAL C 42 0
SHEET 2 Y 4 VAL C 45 ARG C 53 -1 O ASP C 51 N ARG C 35
SHEET 3 Y 4 ILE C 63 SER C 70 -1 O ASP C 64 N ALA C 52
SHEET 4 Y 4 GLU C 78 ILE C 83 -1 O GLN C 80 N ALA C 67
SHEET 1 Z 3 LYS C 146 TRP C 153 0
SHEET 2 Z 3 TRP C 129 ALA C 143 -1 N ALA C 143 O LYS C 146
SHEET 3 Z 3 VAL C 157 SER C 158 -1 O VAL C 157 N LEU C 133
SHEET 1 AA 5 LYS C 146 TRP C 153 0
SHEET 2 AA 5 TRP C 129 ALA C 143 -1 N ALA C 143 O LYS C 146
SHEET 3 AA 5 LYS C 105 TYR C 113 -1 N VAL C 110 O LEU C 132
SHEET 4 AA 5 ARG C 93 LYS C 102 -1 N ILE C 100 O TYR C 107
SHEET 5 AA 5 GLY C 180 VAL C 181 1 O GLY C 180 N VAL C 99
SHEET 1 AB 4 GLU C 166 MET C 167 0
SHEET 2 AB 4 MET C 170 GLY C 177 -1 O MET C 170 N MET C 167
SHEET 3 AB 4 LEU C 190 ASN C 198 -1 O GLN C 195 N LEU C 176
SHEET 4 AB 4 ILE C 183 VAL C 184 -1 N ILE C 183 O VAL C 191
SHEET 1 AC 5 GLU C 166 MET C 167 0
SHEET 2 AC 5 MET C 170 GLY C 177 -1 O MET C 170 N MET C 167
SHEET 3 AC 5 LEU C 190 ASN C 198 -1 O GLN C 195 N LEU C 176
SHEET 4 AC 5 VAL C 203 SER C 210 -1 O PHE C 204 N VAL C 196
SHEET 5 AC 5 LYS C 218 PHE C 219 -1 O LYS C 218 N TYR C 209
SHEET 1 AD 4 CYS C 228 TRP C 236 0
SHEET 2 AD 4 LYS C 239 VAL C 246 -1 O ARG C 245 N SER C 229
SHEET 3 AD 4 VAL C 253 SER C 256 -1 O TYR C 254 N ILE C 242
SHEET 4 AD 4 LEU C 264 GLU C 265 -1 O LEU C 264 N GLU C 255
SHEET 1 AE 4 PHE C 289 ILE C 294 0
SHEET 2 AE 4 MET C 297 PRO C 305 -1 O VAL C 299 N VAL C 292
SHEET 3 AE 4 LEU C 317 THR C 322 -1 O TRP C 320 N PHE C 302
SHEET 4 AE 4 ILE C 327 GLN C 332 -1 O TYR C 328 N LEU C 321
SHEET 1 AF 7 ALA C 446 VAL C 449 0
SHEET 2 AF 7 GLY C 452 PHE C 455 -1 O LYS C 454 N GLU C 447
SHEET 3 AF 7 VAL C 600 TYR C 608 -1 O VAL C 600 N PHE C 455
SHEET 4 AF 7 PHE C 482 ILE C 490 -1 N VAL C 485 O LEU C 606
SHEET 5 AF 7 ARG C 544 ALA C 552 -1 O TYR C 545 N VAL C 488
SHEET 6 AF 7 ILE C 555 ILE C 560 -1 O SER C 557 N THR C 550
SHEET 7 AF 7 GLU C 563 PRO C 564 -1 O GLU C 563 N ILE C 560
SHEET 1 AG13 TRP C 524 TYR C 528 0
SHEET 2 AG13 LYS C 512 ASP C 519 -1 N GLY C 515 O ILE C 527
SHEET 3 AG13 ALA C 497 SER C 504 -1 N LEU C 501 O LEU C 516
SHEET 4 AG13 HIS C 583 VAL C 586 -1 O HIS C 583 N SER C 504
SHEET 5 AG13 GLY C 461 PRO C 465 -1 N TRP C 464 O PHE C 584
SHEET 6 AG13 ALA C 441 ALA C 444 -1 N SER C 442 O LEU C 463
SHEET 7 AG13 GLU C 431 ASP C 434 -1 N TRP C 432 O ALA C 441
SHEET 8 AG13 LEU C 419 ALA C 427 -1 N SER C 426 O GLU C 433
SHEET 9 AG13 VAL C 600 TYR C 608 -1 O VAL C 605 N LEU C 423
SHEET 10 AG13 PHE C 482 ILE C 490 -1 N VAL C 485 O LEU C 606
SHEET 11 AG13 ARG C 544 ALA C 552 -1 O TYR C 545 N VAL C 488
SHEET 12 AG13 ILE C 555 ILE C 560 -1 O SER C 557 N THR C 550
SHEET 13 AG13 GLN C 570 THR C 571 -1 O GLN C 570 N GLY C 556
SHEET 1 AH 4 GLN H 5 GLN H 6 0
SHEET 2 AH 4 VAL H 18 LYS H 23 -1 O LYS H 23 N GLN H 5
SHEET 3 AH 4 THR H 78 LEU H 83 -1 O MET H 81 N MET H 20
SHEET 4 AH 4 VAL H 68 ASP H 73 -1 N THR H 71 O TYR H 80
SHEET 1 AI 6 GLU H 10 VAL H 12 0
SHEET 2 AI 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12
SHEET 3 AI 6 ALA H 92 GLY H 99 -1 N ALA H 92 O LEU H 115
SHEET 4 AI 6 ASP H 32 GLN H 39 -1 N VAL H 37 O TYR H 95
SHEET 5 AI 6 LEU H 45 LEU H 53 -1 O ILE H 48 N TRP H 36
SHEET 6 AI 6 ILE H 58 TYR H 60 -1 O ASN H 59 N ASP H 50
SHEET 1 AJ 4 GLU H 10 VAL H 12 0
SHEET 2 AJ 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12
SHEET 3 AJ 4 ALA H 92 GLY H 99 -1 N ALA H 92 O LEU H 115
SHEET 4 AJ 4 PHE H 106 TRP H 109 -1 O TYR H 108 N ARG H 98
SHEET 1 AK 4 SER H 126 LEU H 130 0
SHEET 2 AK 4 VAL H 142 TYR H 151 -1 O GLY H 145 N LEU H 130
SHEET 3 AK 4 LEU H 180 VAL H 189 -1 O LEU H 183 N VAL H 148
SHEET 4 AK 4 VAL H 169 THR H 171 -1 N HIS H 170 O SER H 186
SHEET 1 AL 4 SER H 126 LEU H 130 0
SHEET 2 AL 4 VAL H 142 TYR H 151 -1 O GLY H 145 N LEU H 130
SHEET 3 AL 4 LEU H 180 VAL H 189 -1 O LEU H 183 N VAL H 148
SHEET 4 AL 4 VAL H 175 GLN H 177 -1 N VAL H 175 O THR H 182
SHEET 1 AM 3 THR H 157 TRP H 160 0
SHEET 2 AM 3 THR H 200 HIS H 205 -1 O ASN H 202 N THR H 159
SHEET 3 AM 3 THR H 210 LYS H 215 -1 O THR H 210 N HIS H 205
SHEET 1 AN 4 LYS I 3 GLN I 6 0
SHEET 2 AN 4 VAL I 18 VAL I 25 -1 O LYS I 23 N GLN I 5
SHEET 3 AN 4 THR I 78 LEU I 83 -1 O MET I 81 N MET I 20
SHEET 4 AN 4 VAL I 68 ASP I 73 -1 N THR I 71 O TYR I 80
SHEET 1 AO 6 GLU I 10 VAL I 12 0
SHEET 2 AO 6 THR I 113 VAL I 117 1 O THR I 116 N VAL I 12
SHEET 3 AO 6 ALA I 92 GLY I 99 -1 N ALA I 92 O LEU I 115
SHEET 4 AO 6 ASP I 32 GLN I 39 -1 N VAL I 37 O TYR I 95
SHEET 5 AO 6 LEU I 45 LEU I 53 -1 O ILE I 51 N ILE I 34
SHEET 6 AO 6 ILE I 58 TYR I 60 -1 O ASN I 59 N ASP I 50
SHEET 1 AP 4 GLU I 10 VAL I 12 0
SHEET 2 AP 4 THR I 113 VAL I 117 1 O THR I 116 N VAL I 12
SHEET 3 AP 4 ALA I 92 GLY I 99 -1 N ALA I 92 O LEU I 115
SHEET 4 AP 4 PHE I 106 TRP I 109 -1 O TYR I 108 N ARG I 98
SHEET 1 AQ 4 SER I 126 LEU I 130 0
SHEET 2 AQ 4 SER I 141 TYR I 151 -1 O GLY I 145 N LEU I 130
SHEET 3 AQ 4 LEU I 180 THR I 190 -1 O LEU I 183 N VAL I 148
SHEET 4 AQ 4 VAL I 169 THR I 171 -1 N HIS I 170 O SER I 186
SHEET 1 AR 4 SER I 126 LEU I 130 0
SHEET 2 AR 4 SER I 141 TYR I 151 -1 O GLY I 145 N LEU I 130
SHEET 3 AR 4 LEU I 180 THR I 190 -1 O LEU I 183 N VAL I 148
SHEET 4 AR 4 VAL I 175 GLN I 177 -1 N VAL I 175 O THR I 182
SHEET 1 AS 3 THR I 157 TRP I 160 0
SHEET 2 AS 3 THR I 200 HIS I 205 -1 O ASN I 202 N THR I 159
SHEET 3 AS 3 THR I 210 LYS I 215 -1 O THR I 210 N HIS I 205
SHEET 1 AT 4 LEU J 4 GLN J 6 0
SHEET 2 AT 4 VAL J 18 ALA J 24 -1 O LYS J 23 N GLN J 5
SHEET 3 AT 4 THR J 78 LEU J 83 -1 O MET J 81 N MET J 20
SHEET 4 AT 4 VAL J 68 ASP J 73 -1 N THR J 71 O TYR J 80
SHEET 1 AU 6 GLU J 10 VAL J 12 0
SHEET 2 AU 6 THR J 113 VAL J 117 1 O THR J 116 N VAL J 12
SHEET 3 AU 6 ALA J 92 GLY J 99 -1 N ALA J 92 O LEU J 115
SHEET 4 AU 6 ASP J 32 GLN J 39 -1 N VAL J 37 O TYR J 95
SHEET 5 AU 6 LEU J 45 LEU J 53 -1 O ILE J 48 N TRP J 36
SHEET 6 AU 6 ILE J 58 TYR J 60 -1 O ASN J 59 N ASP J 50
SHEET 1 AV 4 GLU J 10 VAL J 12 0
SHEET 2 AV 4 THR J 113 VAL J 117 1 O THR J 116 N VAL J 12
SHEET 3 AV 4 ALA J 92 GLY J 99 -1 N ALA J 92 O LEU J 115
SHEET 4 AV 4 PHE J 106 TRP J 109 -1 O TYR J 108 N ARG J 98
SHEET 1 AW 4 SER J 126 LEU J 130 0
SHEET 2 AW 4 SER J 141 TYR J 151 -1 O GLY J 145 N LEU J 130
SHEET 3 AW 4 LEU J 180 THR J 190 -1 O LEU J 183 N VAL J 148
SHEET 4 AW 4 VAL J 169 THR J 171 -1 N HIS J 170 O SER J 186
SHEET 1 AX 4 SER J 126 LEU J 130 0
SHEET 2 AX 4 SER J 141 TYR J 151 -1 O GLY J 145 N LEU J 130
SHEET 3 AX 4 LEU J 180 THR J 190 -1 O LEU J 183 N VAL J 148
SHEET 4 AX 4 VAL J 175 GLN J 177 -1 N VAL J 175 O THR J 182
SHEET 1 AY 3 THR J 157 TRP J 160 0
SHEET 2 AY 3 THR J 200 HIS J 205 -1 O ASN J 202 N THR J 159
SHEET 3 AY 3 THR J 210 LYS J 215 -1 O THR J 210 N HIS J 205
SHEET 1 AZ 4 MET L 4 THR L 5 0
SHEET 2 AZ 4 ILE L 19 ALA L 25 -1 O SER L 24 N THR L 5
SHEET 3 AZ 4 PHE L 69 ILE L 74 -1 O LEU L 72 N LEU L 21
SHEET 4 AZ 4 PHE L 61 SER L 66 -1 N SER L 64 O SER L 71
SHEET 1 BA 6 ILE L 10 SER L 14 0
SHEET 2 BA 6 THR L 101 LYS L 106 1 O GLU L 104 N MET L 11
SHEET 3 BA 6 ASP L 84 GLN L 89 -1 N TYR L 85 O THR L 101
SHEET 4 BA 6 HIS L 33 HIS L 37 -1 N TYR L 35 O TYR L 86
SHEET 5 BA 6 LYS L 44 TYR L 48 -1 O LEU L 46 N TRP L 34
SHEET 6 BA 6 TYR L 52 LEU L 53 -1 O TYR L 52 N TYR L 48
SHEET 1 BB 4 ILE L 10 SER L 14 0
SHEET 2 BB 4 THR L 101 LYS L 106 1 O GLU L 104 N MET L 11
SHEET 3 BB 4 ASP L 84 GLN L 89 -1 N TYR L 85 O THR L 101
SHEET 4 BB 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 89
SHEET 1 BC 4 THR L 113 PHE L 117 0
SHEET 2 BC 4 GLY L 128 PHE L 138 -1 O VAL L 132 N PHE L 117
SHEET 3 BC 4 TYR L 172 THR L 181 -1 O LEU L 178 N VAL L 131
SHEET 4 BC 4 VAL L 158 TRP L 162 -1 N SER L 161 O SER L 175
SHEET 1 BD 4 SER L 152 ARG L 154 0
SHEET 2 BD 4 ASN L 144 ILE L 149 -1 N ILE L 149 O SER L 152
SHEET 3 BD 4 SER L 190 THR L 196 -1 O THR L 192 N LYS L 148
SHEET 4 BD 4 ILE L 204 ASN L 209 -1 O ILE L 204 N ALA L 195
SHEET 1 BE 4 MET M 4 THR M 5 0
SHEET 2 BE 4 ILE M 19 ALA M 25 -1 O SER M 24 N THR M 5
SHEET 3 BE 4 PHE M 69 ILE M 74 -1 O LEU M 72 N LEU M 21
SHEET 4 BE 4 PHE M 61 SER M 66 -1 N SER M 64 O SER M 71
SHEET 1 BF 6 ILE M 10 SER M 14 0
SHEET 2 BF 6 THR M 101 LYS M 106 1 O GLU M 104 N MET M 11
SHEET 3 BF 6 ASP M 84 GLN M 89 -1 N TYR M 85 O THR M 101
SHEET 4 BF 6 HIS M 33 HIS M 37 -1 N HIS M 37 O ASP M 84
SHEET 5 BF 6 LYS M 44 TYR M 48 -1 O LEU M 46 N TRP M 34
SHEET 6 BF 6 TYR M 52 LEU M 53 -1 O TYR M 52 N TYR M 48
SHEET 1 BG 4 ILE M 10 SER M 14 0
SHEET 2 BG 4 THR M 101 LYS M 106 1 O GLU M 104 N MET M 11
SHEET 3 BG 4 ASP M 84 GLN M 89 -1 N TYR M 85 O THR M 101
SHEET 4 BG 4 THR M 96 PHE M 97 -1 O THR M 96 N GLN M 89
SHEET 1 BH 4 THR M 113 PHE M 117 0
SHEET 2 BH 4 GLY M 128 PHE M 138 -1 O VAL M 132 N PHE M 117
SHEET 3 BH 4 TYR M 172 THR M 181 -1 O LEU M 178 N VAL M 131
SHEET 4 BH 4 VAL M 158 TRP M 162 -1 N SER M 161 O SER M 175
SHEET 1 BI 4 SER M 152 ARG M 154 0
SHEET 2 BI 4 ASN M 144 ILE M 149 -1 N TRP M 147 O ARG M 154
SHEET 3 BI 4 SER M 190 THR M 196 -1 O GLU M 194 N LYS M 146
SHEET 4 BI 4 ILE M 204 ASN M 209 -1 O ILE M 204 N ALA M 195
SHEET 1 BJ 4 MET N 4 THR N 5 0
SHEET 2 BJ 4 ILE N 19 ALA N 25 -1 O SER N 24 N THR N 5
SHEET 3 BJ 4 PHE N 69 ILE N 74 -1 O LEU N 72 N LEU N 21
SHEET 4 BJ 4 PHE N 61 SER N 66 -1 N SER N 64 O SER N 71
SHEET 1 BK 6 ILE N 10 SER N 14 0
SHEET 2 BK 6 THR N 101 LYS N 106 1 O GLU N 104 N MET N 11
SHEET 3 BK 6 ASP N 84 GLN N 89 -1 N TYR N 85 O THR N 101
SHEET 4 BK 6 HIS N 33 HIS N 37 -1 N TYR N 35 O TYR N 86
SHEET 5 BK 6 LYS N 44 TYR N 48 -1 O LEU N 46 N TRP N 34
SHEET 6 BK 6 TYR N 52 LEU N 53 -1 O TYR N 52 N TYR N 48
SHEET 1 BL 4 ILE N 10 SER N 14 0
SHEET 2 BL 4 THR N 101 LYS N 106 1 O GLU N 104 N MET N 11
SHEET 3 BL 4 ASP N 84 GLN N 89 -1 N TYR N 85 O THR N 101
SHEET 4 BL 4 THR N 96 PHE N 97 -1 O THR N 96 N GLN N 89
SHEET 1 BM 4 THR N 113 PHE N 117 0
SHEET 2 BM 4 GLY N 128 PHE N 138 -1 O VAL N 132 N PHE N 117
SHEET 3 BM 4 TYR N 172 THR N 181 -1 O LEU N 178 N VAL N 131
SHEET 4 BM 4 VAL N 158 TRP N 162 -1 N SER N 161 O SER N 175
SHEET 1 BN 4 SER N 152 ARG N 154 0
SHEET 2 BN 4 ASN N 144 ILE N 149 -1 N ILE N 149 O SER N 152
SHEET 3 BN 4 SER N 190 THR N 196 -1 O GLU N 194 N LYS N 146
SHEET 4 BN 4 ILE N 204 ASN N 209 -1 O ILE N 204 N ALA N 195
SSBOND 1 CYS A 396 CYS A 410 1555 1555 2.05
SSBOND 2 CYS B 396 CYS B 410 1555 1555 2.06
SSBOND 3 CYS C 396 CYS C 410 1555 1555 2.06
SSBOND 4 CYS H 22 CYS H 96 1555 1555 2.04
SSBOND 5 CYS H 146 CYS H 201 1555 1555 2.03
SSBOND 6 CYS I 22 CYS I 96 1555 1555 2.03
SSBOND 7 CYS I 146 CYS I 201 1555 1555 2.07
SSBOND 8 CYS J 22 CYS J 96 1555 1555 2.03
SSBOND 9 CYS J 146 CYS J 201 1555 1555 2.06
SSBOND 10 CYS L 23 CYS L 87 1555 1555 2.10
SSBOND 11 CYS L 133 CYS L 193 1555 1555 2.04
SSBOND 12 CYS M 23 CYS M 87 1555 1555 2.09
SSBOND 13 CYS M 133 CYS M 193 1555 1555 2.04
SSBOND 14 CYS N 23 CYS N 87 1555 1555 2.07
SSBOND 15 CYS N 133 CYS N 193 1555 1555 2.03
CISPEP 1 PHE H 152 PRO H 153 0 -3.39
CISPEP 2 GLU H 154 PRO H 155 0 3.43
CISPEP 3 TRP H 194 PRO H 195 0 4.10
CISPEP 4 PHE I 152 PRO I 153 0 -3.00
CISPEP 5 GLU I 154 PRO I 155 0 2.52
CISPEP 6 TRP I 194 PRO I 195 0 6.63
CISPEP 7 THR J 28 PHE J 29 0 -12.58
CISPEP 8 PHE J 152 PRO J 153 0 -3.27
CISPEP 9 GLU J 154 PRO J 155 0 2.69
CISPEP 10 TRP J 194 PRO J 195 0 5.93
CISPEP 11 THR L 7 PRO L 8 0 -7.58
CISPEP 12 PHE L 93 PRO L 94 0 -3.16
CISPEP 13 TYR L 139 PRO L 140 0 3.83
CISPEP 14 THR M 7 PRO M 8 0 -7.57
CISPEP 15 PHE M 93 PRO M 94 0 -2.04
CISPEP 16 TYR M 139 PRO M 140 0 3.95
CISPEP 17 THR N 7 PRO N 8 0 -7.68
CISPEP 18 PHE N 93 PRO N 94 0 -2.31
CISPEP 19 TYR N 139 PRO N 140 0 3.95
SITE 1 AC1 2 LYS A 22 ARG A 87
SITE 1 AC2 6 ASP A 59 TYR A 119 ARG A 245 TRP A 312
SITE 2 AC2 6 ARG A 314 TYR A 342
SITE 1 AC3 5 ASP B 59 TYR B 119 GLU B 230 ARG B 245
SITE 2 AC3 5 TYR B 342
CRYST1 178.140 178.140 140.710 90.00 90.00 120.00 P 31 9
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005614 0.003241 0.000000 0.00000
SCALE2 0.000000 0.006482 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007107 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
